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Verfasst von:Tempra, Carmelo [VerfasserIn]   i
 Scollo, Federica [VerfasserIn]   i
 Pannuzzo, Martina [VerfasserIn]   i
 Lolicato, Fabio [VerfasserIn]   i
 La Rosa, Carmelo [VerfasserIn]   i
Titel:A unifying framework for amyloid-mediated membrane damage
Titelzusatz:the lipid-chaperone hypothesis
Verf.angabe:Carmelo Tempra, Federica Scollo, Martina Pannuzzo, Fabio Lolicato, Carmelo La Rosa
E-Jahr:2022
Jahr:8 February 2022
Umfang:13 S.
Fussnoten:Gesehen am 30.08.2022
Titel Quelle:Enthalten in: Biochimica et biophysica acta / Proteins and proteomics
Ort Quelle:Amsterdam [u.a.], 2002
Jahr Quelle:2022
Band/Heft Quelle:1870(2022), 4, Artikel-ID 140767, Seite 1-13
ISSN Quelle:1878-1454
Abstract:Over the past thirty years, researchers have highlighted the role played by a class of proteins or polypeptides that forms pathogenic amyloid aggregates in vivo, including i) the amyloid Aβ peptide, which is known to form senile plaques in Alzheimer's disease; ii) α-synuclein, responsible for Lewy body formation in Parkinson's disease and iii) IAPP, which is the protein component of type 2 diabetes-associated islet amyloids. These proteins, known as intrinsically disordered proteins (IDPs), are present as highly dynamic conformational ensembles. IDPs can partially (mis) fold into (dys) functional conformations and accumulate as amyloid aggregates upon interaction with other cytosolic partners such as proteins or lipid membranes. In addition, an increasing number of reports link the toxicity of amyloid proteins to their harmful effects on membrane integrity. Still, the molecular mechanism underlying the amyloidogenic proteins transfer from the aqueous environment to the hydrocarbon core of the membrane is poorly understood. This review starts with a historical overview of the toxicity models of amyloidogenic proteins to contextualize the more recent lipid-chaperone hypothesis. Then, we report the early molecular-level events in the aggregation and ion-channel pore formation of Aβ, IAPP, and α-synuclein interacting with model membranes, emphasizing the complexity of these processes due to their different spatial-temporal resolutions. Next, we underline the need for a combined experimental and computational approach, focusing on the strengths and weaknesses of the most commonly used techniques. Finally, the last two chapters highlight the crucial role of lipid-protein complexes as molecular switches among ion-channel-like formation, detergent-like, and fibril formation mechanisms and their implication in fighting amyloidogenic diseases.
DOI:doi:10.1016/j.bbapap.2022.140767
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext: https://doi.org/10.1016/j.bbapap.2022.140767
 DOI: https://doi.org/10.1016/j.bbapap.2022.140767
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:Aggregation
 alpha-Synuclein
 Amyloid
 Amyloidogenic Proteins
 Amyloidosis
 Diabetes Mellitus, Type 2
 Humans
 Intrinsically Disordered Proteins
 Ion channel-like
 Lipid-chaperone
 Lipids
 Model membrane
 Molecular Chaperones
 Peptides
 Toxic oligomer
K10plus-PPN:1815384085
Verknüpfungen:→ Zeitschrift

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